1. Consider the following reaction of 1 to 2 below OH cat. HA 2 a. Draw a specific acid-catalyzed mechanism b. Draw a general acid-catalyzed mechanism c. Which acid is more likely to exhibit a general acid mechanism, HCl or acetic acid? Explain your answer in a sentence.
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- Acetazolamide is a drug which inhibits carbonic anhydrase. Carbonic anhydrase participates in regulation of the pH and bicarbonate content of a number of body fluids. Figure 2 shows the experimental curve of initial reaction velocity (as percentage of Vmax) versus [S] (concentration) for the carbonic anhydrase reaction. The graph also shows the curve in the presence of acetazolamide. 100 No inhibitor 50 Acetazolamide 0.2 0.4 0.6 0.8 (S] (mM) Figure 2 (i) Compare the maximal velocities and Michaelis Menten constants of the enzyme in the absence and the presence of the inhibitor acetazolamide. Determine the nature of inhibition by acetazolamide. Explain your answer. (*"A JO %) ABy what factor is sample A2 more concentrated than sample A1?6
- Aerobic degradation of an organic compound by mixed cultureof organism in wastewater can be represented by following reaction. C3H6O3 + a O2 + b NH3 → c C5H7NO2 + d H2o + e CO2 A. Determine a, b, c, d and e, if YX/S = 0.4 d X/g S. B. Determine the yield coefficients YX/O2 and YX/NH3. C. Determine the degree of reductions for the substrate, bacteria and RQ for the organisms4.Pepsin is the proteolytic enzyme of gastric juice. The active form of this enzyme is formed from pepsinogen under HCL action.Optimum of enzyme action: pH = 1.5, t = 37°. Describe the properties of this enzyme. For this:1)Name and explain the mechanism of this enzyme activation.2)Draw the plot and explain the effects of pH and t on the reaction velocity.3) Explain how changes the velocity of this reaction in patients suffering from hypoacidie gastritis.1. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins ofbacterial wall) are 37 C- temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. 2 Consider the matic reaction schee: Asnaragine + H20 Aspartate+ NH3:
- In addition to O, binding, changes in other chemical conditions can result in hemoglobin changes. pH is one of those factors. It can be understood by reaction #1. Red blood cells have the enzyme Carbonic Anhydrase which catalyzes reaction #2. Using the two reactions explain how pH contributes to the transfer of O2 from the lungs to the tissues. H-Hb* + O2 Hb-O2 + H* Reaction #1 CO2(aq) + H2O= H* + HCO3 Reaction #2Draw the major product of the following Suzuki coupling reaction. CN B(OH)2 CI 2 eq K₂CO₂ aq. 3 mol-% Pd(PPh3)4 benzene, A CI Draw the major product of the following Stille coupling reaction. OMe N Bu3Sn + Pd(PPh3)2Cl2 OAC THF, reflux5. Answer the following questions. a. Write the name and structure of the product obtained by the reaction of B-D-glucopyranose with acetic anhydride in the presence of pyridine at 0 °C? (water or ether) b. Which solvent, water or ether, would you prefer to purify the starting material? c. Which solvent is preferred for the purification and recrystallization of the final product from the reaction.
- Give a complete and well descriptive definition of the following:1.1 Fractional saturation1.2Allostery1.3 Metal activated enzymes 1.4 Metalloenzymes1.5 Acid-base catalysisA researcher wants to look for glucaronic acid conjugated metabolites in sample of urine(glucaronic acid conjugation is a common method of metabolism for excretion.) Pronotated glucaronic acid conjugated metabolite ions often lose anhydroglucaronic acid(176 Da) during low energy CID. Which triple quadrupole experiment might be best for finding these conjugates?Carbonic anhydrase catalyzes the hydration of CO. CO2 + H2O ¬ H½CO3 The Km of this enzyme for CO, is 1.20×104 µ.M. When [CO,] = 3.60×104 µM, the rate of reaction was 4.50 umol·mL! sec-1 a What is Vmax for this enzyme? umol·mL-!sec-!